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Crystallization and preliminary X‐ray diffraction studies of the C‐terminal domain of Chlamydia trachomatis CdsD
Author(s) -
Meriläinen Gitte,
Wierenga Rik K.
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14019712
Subject(s) - chlamydia trachomatis , crystallization , amino acid , escherichia coli , chemistry , resolution (logic) , ring (chemistry) , crystallography , stereochemistry , biology , gene , biochemistry , organic chemistry , artificial intelligence , computer science , immunology
The inner membrane ring of the bacterial type III secretion system (TTSS) is composed of two proteins. In Chlamydia trachomatis this ring is formed by CdsD (gene name CT_664 ) and CdsJ (gene name CTA_0609 ). CdsD consists of 829 amino acids. The last 400 amino acids at its C‐terminal end relate it to the type III secretion system YscD/HrpQ protein family. The C‐terminal domain, consisting of amino acids 558–771, of C. trachomatis CdsD was overexpressed in Escherichia coli and purified using immobilized metal‐affinity chromatography (IMAC) and size‐exclusion chromatography. The protein was crystallized using the vapour‐diffusion method. A data set was collected to 2.26 Å resolution. The crystals have the symmetry of space group C 2, with unit‐cell parameters a = 106.60, b = 23.91, c = 118.65 Å, β = 104.95°. According to the data analysis there is expected to be one molecule in the asymmetric unit, with a Matthews coefficient of 3.0 Å 3 Da −1 .